5frt: Difference between revisions

Latest revision as of 18:23, 8 September 2026

Structure of the FeSII (shethna) protein of Azotobacter vinelandii

Structural highlights

5frt is a 5 chain structure with sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.34Å
Ligands:	FES
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FESII_AZOVI Binds to and protects nitrogenase from irreversible exposure to O(2), in what is known as 'conformational protection' (PubMed:10220344, PubMed:26654855, PubMed:7548055, PubMed:7830548). Shifts nitrogenase into an inactive, O(2)-tolerant state. Exists in 2 states, an open oxidized state that binds and protects nitrogenase, and a closed reduced state that probably does not bind nitrogenase; cooperative oxidation of the 2Fe-2S clusters causes the conformation change (PubMed:26654855). Does not protect nitrogenase with the vanadium-iron subunit, not clear if it protects the iron-only nitrogenase (PubMed:7830548).^[1] ^[2] ^[3] ^[4]

References

↑ Lou J, Moshiri F, Johnson MK, Lafferty ME, Sorkin DL, Miller A, Maier RJ. Mutagenesis studies of the FeSII protein of Azotobacter vinelandii: roles of histidine and lysine residues in the protection of nitrogenase from oxygen damage. Biochemistry. 1999 Apr 27;38(17):5563-71. PMID:10220344 doi:10.1021/bi9827823
↑ Schlesier J, Rohde M, Gerhardt S, Einsle O. A Conformational Switch Triggers Nitrogenase Protection from Oxygen Damage by Shethna Protein II (FeSII). J Am Chem Soc. 2015 Dec 24. PMID:26654855 doi:https://dx.doi.org/10.1021/jacs.5b10341
↑ Moshiri F, Crouse BR, Johnson MK, Maier RJ. The "nitrogenase-protective" FeSII protein of Azotobacter vinelandii: overexpression, characterization, and crystallization. Biochemistry. 1995 Oct 10;34(40):12973-82. PMID:7548055 doi:10.1021/bi00040a007
↑ Moshiri F, Kim JW, Fu C, Maier RJ. The FeSII protein of Azotobacter vinelandii is not essential for aerobic nitrogen fixation, but confers significant protection to oxygen-mediated inactivation of nitrogenase in vitro and in vivo. Mol Microbiol. 1994 Oct;14(1):101-14. PMID:7830548 doi:10.1111/j.1365-2958.1994.tb01270.x

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OCA

[1] Lou J, Moshiri F, Johnson MK, Lafferty ME, Sorkin DL, Miller A, Maier RJ. Mutagenesis studies of the FeSII protein of Azotobacter vinelandii: roles of histidine and lysine residues in the protection of nitrogenase from oxygen damage. Biochemistry. 1999 Apr 27;38(17):5563-71. PMID:10220344 doi:10.1021/bi9827823

[2] Schlesier J, Rohde M, Gerhardt S, Einsle O. A Conformational Switch Triggers Nitrogenase Protection from Oxygen Damage by Shethna Protein II (FeSII). J Am Chem Soc. 2015 Dec 24. PMID:26654855 doi:https://dx.doi.org/10.1021/jacs.5b10341

[3] Moshiri F, Crouse BR, Johnson MK, Maier RJ. The "nitrogenase-protective" FeSII protein of Azotobacter vinelandii: overexpression, characterization, and crystallization. Biochemistry. 1995 Oct 10;34(40):12973-82. PMID:7548055 doi:10.1021/bi00040a007

[4] Moshiri F, Kim JW, Fu C, Maier RJ. The FeSII protein of Azotobacter vinelandii is not essential for aerobic nitrogen fixation, but confers significant protection to oxygen-mediated inactivation of nitrogenase in vitro and in vivo. Mol Microbiol. 1994 Oct;14(1):101-14. PMID:7830548 doi:10.1111/j.1365-2958.1994.tb01270.x

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 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/FESII_AZOVI FESII_AZOVI] Binds to and protects nitrogenase from irreversible exposure to O(2), in what is known as 'conformational protection' (PubMed:7830548, PubMed:7548055, PubMed:10220344, PubMed:26654855). Shifts nitrogenase into an inactive, O(2)-tolerant state. Exists in 2 states, an open oxidized state that binds and protects nitrogenase, and a closed reduced state that probably does not bind nitrogenase; cooperative oxidation of the 2Fe-2S clusters causes the conformation change (PubMed:26654855). Does not protect nitrogenase with the vanadium-iron subunit, not clear if it protects the iron-only nitrogenase (PubMed:7830548).<ref>PMID:10220344</ref> <ref>PMID:26654855</ref> <ref>PMID:7548055</ref> <ref>PMID:7830548</ref>
+[https://www.uniprot.org/uniprot/FESII_AZOVI FESII_AZOVI] Binds to and protects nitrogenase from irreversible exposure to O(2), in what is known as 'conformational protection' (PubMed:10220344, PubMed:26654855, PubMed:7548055, PubMed:7830548). Shifts nitrogenase into an inactive, O(2)-tolerant state. Exists in 2 states, an open oxidized state that binds and protects nitrogenase, and a closed reduced state that probably does not bind nitrogenase; cooperative oxidation of the 2Fe-2S clusters causes the conformation change (PubMed:26654855). Does not protect nitrogenase with the vanadium-iron subunit, not clear if it protects the iron-only nitrogenase (PubMed:7830548).<ref>PMID:10220344</ref> <ref>PMID:26654855</ref> <ref>PMID:7548055</ref> <ref>PMID:7830548</ref>
 == References ==
 <references/>

5frt: Difference between revisions

Latest revision as of 18:23, 8 September 2026

Structure of the FeSII (shethna) protein of Azotobacter vinelandii

Structural highlights

Function

References

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